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Front Cover: From Natural Methylation to Versatile Alkylations Using Halide Methyltransferases (ChemBioChem 16/2021)
Author(s) -
Tang Qingyun,
Pavlidis Ioannis V.,
Badenhorst Christoffel P. S.,
Bornscheuer Uwe T.
Publication year - 2021
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.202100259
Subject(s) - methyltransferase , halide , methylation , chemistry , alkyl , alkylation , regioselectivity , combinatorial chemistry , methionine , stereochemistry , amino acid , organic chemistry , biochemistry , dna , catalysis
The evolution of promiscuous halide methyltransferases enables the enzymatic synthesis of S ‐adenosyl‐ l ‐methionine analogues from alkyl iodides and S ‐adenosyl‐ l ‐homocysteine. This facilitates the synthesis of analogues with alkyl groups larger than methyl groups, which can readily be used by methyltransferases. These processes provide access to diverse alkylated products with altered bioactivities, expanding the synthetic potential of methyltransferases. We expect a toolbox of protein‐engineered halide methyltransferase variants to pave the way towards versatile chemo‐ and regioselective biocatalytic alkylations. More information can be found in the Concept article by C. P. S. Badenhorst, U. T. Bornscheuer et al.